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UniProtKB/Swiss-Prot entry P31948


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name STIP1_HUMAN
Primary accession number P31948
Secondary accession number Q5TZU9
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Stress-induced-phosphoprotein 1
Synonyms STI1
Hsc70/Hsp90-organizing protein
Hop
Transformation-sensitive protein IEF SSP 3521
NY-REN-11 antigen
Gene name
Name: STIP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1569099 [NCBI, ExPASy, EBI, Israel, Japan]
Honore B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.;
"Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1.";
J. Biol. Chem. 267:8485-8491(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-10; 110-118; 345-364; 382-389; 479-486 AND 534-543, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 33-44, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[10]
INTERACTION WITH PACRG.
DOI=10.1074/jbc.M309655200; PubMed=14532270 [NCBI, ExPASy, EBI, Israel, Japan]
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.";
J. Biol. Chem. 278:51901-51910(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-481, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349.
DOI=10.1016/S0092-8674(00)80830-2; PubMed=10786835 [NCBI, ExPASy, EBI, Israel, Japan]
Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I.;
"Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.";
Cell 101:199-210(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M86752; AAA58682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020010; AAV38813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020011; AAV38814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536512; CAG38750.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471076; EAW74196.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002987; AAH02987.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38093; A38093.
RefSeq NP_006810.1; -.
UniGene Hs.337295
3D structure databases
PDB
1ELR; X-ray; 1.90 A; A=223-352.[ExPASy / RCSB / EBI]
1ELW; X-ray; 1.60 A; A/B=1-118.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ELR; -.
1ELW; -.
ModBase P31948.
Protein-protein interaction databases
IntAct P31948; -.
PTM databases
PhosphoSite P31948; -.
2D gel databases
Aarhus/Ghent-2DPAGE 2410; IEF.
REPRODUCTION-2DPAGE IPI00013894; -.
Organism-specific databases
H-InvDB HIX0019658; -.
HGNC HGNC:11387; STIP1.
GenAtlas STIP1.
MIM 605063; gene. [NCBI / EBI]
PharmGKB PA36196; -.
GeneCards P31948.
Gene expression databases
ArrayExpress P31948; -.
CleanEx HS_STIP1; -.
GermOnline ENSG00000168439; Homo sapiens.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (traceable author statement from UniProtKB).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0006950; Biological process: response to stress (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR006636; STI1_HS_bd.
IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 2.
Pfam PF00515; TPR_1; 9.
Pfam graphical view of domain structure.
SMART SM00727; STI1; 2.
SM00028; TPR; 9.
SMART graphical view of domain structure.
PROSITE PS50005; TPR; 9.
PS50293; TPR_REGION; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P31948.
ProtoNet P31948.
Genome annotation databases
Ensembl ENSG00000168439; Homo sapiens. [Contig view]
GeneID 10963; -.
KEGG hsa:10963; -.
Phylogenomic databases
HOVERGEN P31948; -.
Other
LinkHub P31948; -.
NextBio 41662; -.
SOURCE STIP1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Repeat; TPR repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   543  543     Stress-induced-phosphoprotein 1. PRO_0000106372
REPEAT   4    37  34     TPR 1. 
REPEAT   38    71  34     TPR 2. 
REPEAT   72   105  34     TPR 3. 
DOMAIN   130   169  40     STI1 1. 
REPEAT   225   258  34     TPR 4. 
REPEAT   259   292  34     TPR 5. 
REPEAT   300   333  34     TPR 6. 
REPEAT   360   393  34     TPR 7. 
REPEAT   394   427  34     TPR 8. 
REPEAT   428   461  34     TPR 9. 
DOMAIN   492   531  40     STI1 2. 
MOTIF   222   239  18     Bipartite nuclear localization signal (Potential). 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   16    16        Phosphoserine. 
MOD_RES   198   198        Phosphothreonine. 
MOD_RES   246   246        N6-acetyllysine. 
MOD_RES   354   354        Phosphotyrosine. 
MOD_RES   481   481        Phosphoserine. 
HELIX   3    16  14      
HELIX   20    33  14      
HELIX   38    51  14      
HELIX   54    67  14      
HELIX   72    84  13      
HELIX   88    99  12      
HELIX   106   117  12      
HELIX   223   237  15      
HELIX   241   254  14      
HELIX   259   272  14      
HELIX   275   291  17      
HELIX   296   312  17      
HELIX   316   329  14      
HELIX   333   348  16      
Sequence information
Length: 543 AA [This is the length of the unprocessed precursor] Molecular weight: 62639 Da [This is the MW of the unprocessed precursor] CRC64: 8E58ECA13825CB0E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED 

        70         80         90        100        110        120 
GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA 

       130        140        150        160        170        180 
ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS 

       190        200        210        220        230        240 
VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD 

       250        260        270        280        290        300 
FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA 

       310        320        330        340        350        360 
KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA 

       370        380        390        400        410        420 
LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC 

       430        440        450        460        470        480 
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD 

       490        500        510        520        530        540 
SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI 


AIR 

P31948 in FASTA format

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